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Human transthyretin (ttr) complexed with bivalant amyloid inhibitor (4 carbon linker)

Analyse Human transthyretin (ttr) complexed with bivalant amyloid inhibitor (4 carbon… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FBR
Type: protein
Length: 229 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Ligands: 44C
Pockets: 2 · best druggability 0.35

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transthyretin	protein	115	6% helix, 53% strand	P02766
B	Transthyretin	protein	114	6% helix, 50% strand	P02766

Ligands and binding sites

44C · 4'-(4-{4-[(2-carboxyphenyl)amino]phenoxy}butoxy)-1,1'-biphenyl-4-carboxylic acid · ligand · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	84	0.35	0.75	16	empty
2	63	0.31	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 914 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

2FBR · Human transthyretin (TTR) complexed with bivalant amyloid inhibitor (4 carbon linker) · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P02766
Elsewhere: RCSB PDB 2FBR · PDBe 2FBR · UniProt P02766

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